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POU domain, class 4, transcription factor 2 (Brain-specific homeobox/POU domain protein 3B) (Brain-3B) (Brn-3B) (Brn-3.2)

 PO4F2_MOUSE             Reviewed;         411 AA.
Q63934; Q63954;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 138.
RecName: Full=POU domain, class 4, transcription factor 2 {ECO:0000312|MGI:MGI:102524};
AltName: Full=Brain-specific homeobox/POU domain protein 3B;
Short=Brain-3B;
Short=Brn-3B;
AltName: Full=Brn-3.2 {ECO:0000303|PubMed:7904822};
Name=Pou4f2 {ECO:0000312|MGI:MGI:102524};
Synonyms=Brn-3.2 {ECO:0000303|PubMed:7904822}, Brn3b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DNA-BINDING, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=7904822; DOI=10.1016/0896-6273(94)90164-3;
Turner E.E., Jenne K.J., Rosenfeld M.G.;
"Brn-3.2: a Brn-3-related transcription factor with distinctive
central nervous system expression and regulation by retinoic acid.";
Neuron 12:205-218(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
STRAIN=CD;
PubMed=8162704;
Theil T., Zechner U., Klett C., Adolph S., Moeroey T.;
"Chromosomal localization and sequences of the murine Brn-3 family of
developmental control genes.";
Cytogenet. Cell Genet. 66:267-271(1994).
[4]
DNA-BINDING (ISOFORM 2), AND DEVELOPMENTAL STAGE.
PubMed=8290353; DOI=10.1093/nar/21.25.5921;
Theil T., McLean-Hunter S., Zoernig M., Moeroey T.;
"Mouse Brn-3 family of POU transcription factors: a new aminoterminal
domain is crucial for the oncogenic activity of Brn-3a.";
Nucleic Acids Res. 21:5921-5929(1993).
[5]
FUNCTION (ISOFORMS 2), AND INDUCTION.
PubMed=8065921; DOI=10.1093/nar/22.15.3092;
Budhram-Mahadeo V., Theil T., Morris P.J., Lillycrop K.A., Moroy T.,
Latchman D.S.;
"The DNA target site for the Brn-3 POU family transcription factors
can confer responsiveness to cyclic AMP and removal of serum in
neuronal cells.";
Nucleic Acids Res. 22:3092-3098(1994).
[6]
FUNCTION (ISOFORM 2), INTERACTION WITH POU4F1 (ISOFORM 2), AND
DEVELOPMENTAL STAGE.
PubMed=8537352; DOI=10.1074/jbc.270.52.30958;
Theil T., Roedel B., Spiegelhalter F., Moeroey T.;
"Short isoform of POU factor Brn-3b can form a heterodimer with Brn-3a
that is inactive for octamer motif binding.";
J. Biol. Chem. 270:30958-30964(1995).
[7]
DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=8637595; DOI=10.1038/381603a0;
Erkman L., McEvilly R.J., Luo L., Ryan A.K., Hooshmand F.,
O'Connell S.M., Keithley E.M., Rapaport D.H., Ryan A.F.,
Rosenfeld M.G.;
"Role of transcription factors Brn-3.1 and Brn-3.2 in auditory and
visual system development.";
Nature 381:603-606(1996).
[8]
TISSUE SPECIFICITY.
TISSUE=Retina;
PubMed=7691107; DOI=10.1016/0896-6273(93)90079-7;
Xiang M., Zhou L.-J., Peng Y., Eddy R.L., Shows T.B., Nathans J.;
"Brn-3b: a POU domain gene expressed in a subset of retinal ganglion
cells.";
Neuron 11:689-701(1993).
[9]
FUNCTION (ISOFORM 2), AND DNA-BINDING (ISOFORM 2).
PubMed=7935408; DOI=10.1128/MCB.14.10.6907;
Morris P.J., Theil T., Ring C.J., Lillycrop K.A., Moroy T.,
Latchman D.S.;
"The opposite and antagonistic effects of the closely related POU
family transcription factors Brn-3a and Brn-3b on the activity of a
target promoter are dependent on differences in the POU domain.";
Mol. Cell. Biol. 14:6907-6914(1994).
[10]
FUNCTION (ISOFORM 2).
PubMed=7852360; DOI=10.1074/jbc.270.6.2853;
Budhram-Mahadeo V., Morris P.J., Lakin N.D., Theil T., Ching G.Y.,
Lillycrop K.A., Moeroey T., Liem R.K., Latchman D.S.;
"Activation of the alpha-internexin promoter by the Brn-3a
transcription factor is dependent on the N-terminal region of the
protein.";
J. Biol. Chem. 270:2853-2858(1995).
[11]
FUNCTION (ISOFORM 2).
PubMed=7797498; DOI=10.1074/jbc.270.25.15143;
Milton N.G., Bessis A., Changeux J.P., Latchman D.S.;
"The neuronal nicotinic acetylcholine receptor alpha 2 subunit gene
promoter is activated by the Brn-3b POU family transcription factor
and not by Brn-3a or Brn-3c.";
J. Biol. Chem. 270:15143-15147(1995).
[12]
FUNCTION (ISOFORM 1), AND MUTAGENESIS OF ILE-368.
PubMed=8662774; DOI=10.1074/jbc.271.20.11897;
Dawson S.J., Morris P.J., Latchman D.S.;
"A single amino acid change converts an inhibitory transcription
factor into an activator.";
J. Biol. Chem. 271:11631-11633(1996).
[13]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=8632990; DOI=10.1073/pnas.93.9.3920;
Gan L., Xiang M., Zhou L., Wagner D.S., Klein W.H., Nathans J.;
"POU domain factor Brn-3b is required for the development of a large
set of retinal ganglion cells.";
Proc. Natl. Acad. Sci. U.S.A. 93:3920-3925(1996).
[14]
FUNCTION, INDUCTION, MUTAGENESIS OF ILE-368, AND DOMAIN.
PubMed=8995448; DOI=10.1074/jbc.272.2.1382;
Smith M.D., Dawson S.J., Latchman D.S.;
"Inhibition of neuronal process outgrowth and neuronal specific gene
activation by the Brn-3b transcription factor.";
J. Biol. Chem. 272:1382-1388(1997).
[15]
FUNCTION, AND MUTAGENESIS OF ILE-368.
PubMed=9261145; DOI=10.1074/jbc.272.34.21325;
Smith M.D., Morris P.J., Dawson S.J., Schwartz M.L., Schlaepfer W.W.,
Latchman D.S.;
"Coordinate induction of the three neurofilament genes by the Brn-3a
transcription factor.";
J. Biol. Chem. 272:21325-21333(1997).
[16]
FUNCTION, AND MUTAGENESIS OF ILE-368.
PubMed=8972215; DOI=10.1128/MCB.17.1.345;
Smith M.D., Dawson S.J., Latchman D.S.;
"The Brn-3a transcription factor induces neuronal process outgrowth
and the coordinate expression of genes encoding synaptic proteins.";
Mol. Cell. Biol. 17:345-354(1997).
[17]
DNA-BINDING.
PubMed=9111308; DOI=10.1128/MCB.17.5.2391;
Gruber C.A., Rhee J.M., Gleiberman A., Turner E.E.;
"POU domain factors of the Brn-3 class recognize functional DNA
elements which are distinctive, symmetrical, and highly conserved in
evolution.";
Mol. Cell. Biol. 17:2391-2400(1997).
[18]
FUNCTION (ISOFORM 2), AND INTERACTION WITH ESR1 (ISOFORM 2).
PubMed=9448000; DOI=10.1128/MCB.18.2.1029;
Budhram-Mahadeo V., Parker M., Latchman D.S.;
"POU transcription factors Brn-3a and Brn-3b interact with the
estrogen receptor and differentially regulate transcriptional activity
via an estrogen response element.";
Mol. Cell. Biol. 18:1029-1041(1998).
[19]
FUNCTION (ISOFORM 2), AND MUTAGENESIS OF ILE-368.
PubMed=9694219;
Dawson S.J., Palmer R.D., Morris P.J., Latchman D.S.;
"Functional role of position 22 in the homeodomain of Brn-3
transcription factors.";
NeuroReport 9:2305-2309(1998).
[20]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10357904; DOI=10.1006/dbio.1999.9280;
Gan L., Wang S.W., Huang Z., Klein W.H.;
"POU domain factor Brn-3b is essential for retinal ganglion cell
differentiation and survival but not for initial cell fate
specification.";
Dev. Biol. 210:469-480(1999).
[21]
FUNCTION (ISOFORM 1).
PubMed=10526314;
Plaza S., Hennemann H., Moeroey T., Saule S., Dozier C.;
"Evidence that POU factor Brn-3B regulates expression of Pax-6 in
neuroretina cells.";
J. Neurobiol. 41:349-358(1999).
[22]
FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORM 1), AND DEVELOPMENTAL
STAGE.
PubMed=10414983;
Trieu M., Rhee J.M., Fedtsova N., Turner E.E.;
"Autoregulatory sequences are revealed by complex stability screening
of the mouse brn-3.0 locus.";
J. Neurosci. 19:6549-6558(1999).
[23]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11163266; DOI=10.1016/S0896-6273(00)00153-7;
Erkman L., Yates P.A., McLaughlin T., McEvilly R.J., Whisenhunt T.,
O'Connell S.M., Krones A.I., Kirby M.A., Rapaport D.H.,
Bermingham J.R. Jr., O'Leary D.D.M., Rosenfeld M.G.;
"A POU domain transcription factor-dependent program regulates axon
pathfinding in the vertebrate visual system.";
Neuron 28:779-792(2000).
[24]
FUNCTION (ISOFORM 2).
PubMed=11526481; DOI=10.1038/sj.onc.1204491;
Dennis J.H., Budhram-Mahadeo V., Latchman D.S.;
"The Brn-3b POU family transcription factor regulates the cellular
growth, proliferation, and anchorage dependence of MCF7 human breast
cancer cells.";
Oncogene 20:4961-4971(2001).
[25]
FUNCTION (ISOFORMS 1 AND 2).
PubMed=14726699; DOI=10.4161/cbt.3.3.698;
Samady L., Dennis J., Budhram-Mahadeo V., Latchman D.S.;
"Activation of CDK4 gene expression in human breast cancer cells by
the Brn-3b POU family transcription factor.";
Cancer Biol. Ther. 3:317-323(2004).
[26]
FUNCTION (ISOFORM 1), AND DOMAIN (ISOFORM 1).
PubMed=15733064; DOI=10.1111/j.1432-0436.2005.07301004.x;
Martin S.E., Mu X., Klein W.H.;
"Identification of an N-terminal transcriptional activation domain
within Brn3b/POU4f2.";
Differentiation 73:18-27(2005).
[27]
FUNCTION (ISOFORMS 1 AND 2), DNA-BINDING, AND TISSUE SPECIFICITY.
PubMed=16152597; DOI=10.1002/ijc.21435;
Samady L., Faulkes D.J., Budhram-Mahadeo V., Ndisang D., Potter E.,
Brabant G., Latchman D.S.;
"The Brn-3b POU family transcription factor represses plakoglobin gene
expression in human breast cancer cells.";
Int. J. Cancer 118:869-878(2006).
[28]
FUNCTION (ISOFORM 2), INTERACTION WITH TP53 (ISOFORM 2), AND CHROMATIN
BINDING (ISOFORM 2).
PubMed=17145718; DOI=10.1093/nar/gkl878;
Budhram-Mahadeo V.S., Bowen S., Lee S., Perez-Sanchez C., Ensor E.,
Morris P.J., Latchman D.S.;
"Brn-3b enhances the pro-apoptotic effects of p53 but not its
induction of cell cycle arrest by cooperating in trans-activation of
bax expression.";
Nucleic Acids Res. 34:6640-6652(2006).
[29]
FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
INDUCTION.
PubMed=17668438; DOI=10.1002/jcb.21257;
Schulze-Spaete U., Battaglino R., Fu J., Sharma A., Vokes M.,
Stashenko P.;
"Brn3 transcription factors control terminal osteoclastogenesis.";
J. Cell. Biochem. 102:1-12(2007).
[30]
FUNCTION (ISOFORM 1), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE
(ISOFORMS 1 AND 2).
PubMed=18368538; DOI=10.1007/s12192-008-0028-2;
Farooqui-Kabir S.R., Diss J.K., Henderson D., Marber M.S.,
Latchman D.S., Budhram-Mahadeo V., Heads R.J.;
"Cardiac expression of Brn-3a and Brn-3b POU transcription factors and
regulation of Hsp27 gene expression.";
Cell Stress Chaperones 13:297-312(2008).
[31]
FUNCTION (ISOFORM 1), INTERACTION WITH DLX1 AND DLX2 (ISOFORM 1),
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=21875655; DOI=10.1016/j.neuroscience.2011.08.015;
Feng L., Eisenstat D.D., Chiba S., Ishizaki Y., Gan L., Shibasaki K.;
"Brn-3b inhibits generation of amacrine cells by binding to and
negatively regulating DLX1/2 in developing retina.";
Neuroscience 195:9-20(2011).
[32]
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=22326227; DOI=10.1016/j.ydbio.2012.01.021;
Zou M., Li S., Klein W.H., Xiang M.;
"Brn3a/Pou4f1 regulates dorsal root ganglion sensory neuron
specification and axonal projection into the spinal cord.";
Dev. Biol. 364:114-127(2012).
[33]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23805044;
Zhang L., Wahlin K., Li Y., Masuda T., Yang Z., Zack D.J., Esumi N.;
"RIT2, a neuron-specific small guanosine triphosphatase, is expressed
in retinal neuronal cells and its promoter is modulated by the POU4
transcription factors.";
Mol. Vis. 19:1371-1386(2013).
[34]
FUNCTION (ISOFORM 1), INTERACTION WITH ISL1; ISL2 AND LHX2 (ISOFORM
1), DNA-BINDING (ISOFORM 1), CHROMATIN BINDING (ISOFORM 1), AND
DISRUPTION PHENOTYPE.
PubMed=24643061; DOI=10.1371/journal.pone.0092105;
Li R., Wu F., Ruonala R., Sapkota D., Hu Z., Mu X.;
"Isl1 and Pou4f2 form a complex to regulate target genes in developing
retinal ganglion cells.";
PLoS ONE 9:E92105-E92105(2014).
[35]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25775587; DOI=10.1073/pnas.1421535112;
Wu F., Kaczynski T.J., Sethuramanujam S., Li R., Jain V.,
Slaughter M., Mu X.;
"Two transcription factors, Pou4f2 and Isl1, are sufficient to specify
the retinal ganglion cell fate.";
Proc. Natl. Acad. Sci. U.S.A. 112:E1559-E1568(2015).
-!- FUNCTION: DNA-binding transcriptional regulator and coregulator
that recognizes and binds to the consensus octamer binding site
5'-AT[A/T]A[T/A]T[A/T]A-3' in promoter of target genes
(PubMed:7904822, PubMed:8290353, PubMed:7935408, PubMed:9111308,
PubMed:10414983, PubMed:16152597, PubMed:17145718,
PubMed:17668438, PubMed:21875655, PubMed:24643061). Plays a
fundamental role in the gene regulatory network essential for
retinal ganglion cell (RGC) differentiation (PubMed:8632990,
PubMed:24643061, PubMed:25775587). Cooperates with the
transcription factor ISL1 to achieve RGC fate specification in the
developing retina (PubMed:25775587). Plays also a role in RGC axon
formation and guidance by regulating gene expression of specific
target genes (PubMed:8995448, PubMed:9261145, PubMed:8972215,
PubMed:10357904, PubMed:11163266). Plays a role in TNFSF11-
mediated terminal osteoclast differentiation (PubMed:17668438).
Binds chromatin at promoter region of target genes
(PubMed:17145718, PubMed:24643061). {ECO:0000269|PubMed:10357904,
ECO:0000269|PubMed:10414983, ECO:0000269|PubMed:11163266,
ECO:0000269|PubMed:16152597, ECO:0000269|PubMed:17145718,
ECO:0000269|PubMed:17668438, ECO:0000269|PubMed:21875655,
ECO:0000269|PubMed:24643061, ECO:0000269|PubMed:25775587,
ECO:0000269|PubMed:7904822, ECO:0000269|PubMed:7935408,
ECO:0000269|PubMed:8290353, ECO:0000269|PubMed:8632990,
ECO:0000269|PubMed:8972215, ECO:0000269|PubMed:8995448,
ECO:0000269|PubMed:9111308, ECO:0000269|PubMed:9261145}.
-!- FUNCTION: Isoform 1: Acts either as a transcriptional activator or
repressor (PubMed:7904822, PubMed:8662774, PubMed:10526314,
PubMed:10414983, PubMed:14726699, PubMed:15733064,
PubMed:16152597, PubMed:18368538, PubMed:21875655,
PubMed:24643061). Negatively regulates transcriptional activity of
homeobox domain transcriptional factors DLX1 and DLX2, and hence
prevents DLX1- and DLX2-mediated ability to promote amacrine cells
specification (PubMed:21875655). Involved in the positive
regulation of the transcriptional factor PAX6 expression through
its binding to the neuroretina-specific enhancer in neuroretina
cells (PubMed:10526314). Mediates positive transcriptional
regulation of heat shock protein HSPB1 expression in cardiac
myocytes (PubMed:18368538). Positively regulates POU4F1 expression
by interacting directly with a highly conserved autoregulatory
domain surrounding the transcription initiation site of the POU4F1
gene promoter (PubMed:10414983). Plays a role in the regulation of
breast cancer cell growth by promoting transcription activation as
well as repression of specific target genes (PubMed:14726699,
PubMed:16152597). Involved in tumor breast progression and
invasion (PubMed:16152597). Plays also a role either as a
transcriptional coactivator or corepressor (PubMed:8662774,
PubMed:24643061). Transcriptional coactivator cooperating with
transcription factors ISL1 and ISL2 to potentiate transcriptional
activation of retinal ganglion cell (RGC) target genes
(PubMed:24643061). Antagonizes the transcriptional stimulatory
activity of POU4F1 by preventing its binding to the octamer motif
(PubMed:8662774). Binds to the octamer binding site to form a
ternary complex with ISL1 in promoter of target genes
(PubMed:24643061). {ECO:0000269|PubMed:10414983,
ECO:0000269|PubMed:10526314, ECO:0000269|PubMed:14726699,
ECO:0000269|PubMed:15733064, ECO:0000269|PubMed:16152597,
ECO:0000269|PubMed:18368538, ECO:0000269|PubMed:21875655,
ECO:0000269|PubMed:24643061, ECO:0000269|PubMed:7904822,
ECO:0000269|PubMed:8662774}.
-!- FUNCTION: Isoform 2: Acts either as a transcriptional activator or
repressor (PubMed:8065921, PubMed:7935408, PubMed:7797498,
PubMed:9694219, PubMed:14726699, PubMed:16152597,
PubMed:17145718). Stimulates the promoter activity of the neuronal
nicotinic acetylcholine receptor alpha CHRNA2 (PubMed:7797498).
Negatively regulates the apoptosis regulator BAX promoter activity
(PubMed:17145718). Inhibits promoter activity of the neuronal
intermediate filament protein alpha-internexin INA gene
(PubMed:7852360). Plays a role in the regulation of breast cancer
cell growth by promoting transcription activation as well as
repression of specific target genes (PubMed:14726699,
PubMed:16152597). Involved in tumor breast progression and
invasion (PubMed:11526481, PubMed:16152597). Plays also a role
either as a transcriptional coactivator or corepressor
(PubMed:8537352, PubMed:7935408, PubMed:7852360, PubMed:9448000,
PubMed:17145718). Transcriptional coactivator cooperating with
transcription factors TP53 to potentiate transcriptional
activation of BAX promoter activity, and hence increases neuronal
cell apoptosis (PubMed:17145718). Antagonizes the transcriptional
stimulatory activity of POU4F1 by preventing its binding to the
octamer motif (PubMed:8537352, PubMed:7935408, PubMed:7852360).
Acts also as a transcriptional coactivator via its interaction
with the transcription factor ESR1 (PubMed:9448000).
{ECO:0000269|PubMed:11526481, ECO:0000269|PubMed:14726699,
ECO:0000269|PubMed:16152597, ECO:0000269|PubMed:17145718,
ECO:0000269|PubMed:7797498, ECO:0000269|PubMed:7852360,
ECO:0000269|PubMed:7935408, ECO:0000269|PubMed:8065921,
ECO:0000269|PubMed:8537352, ECO:0000269|PubMed:9448000,
ECO:0000269|PubMed:9694219}.
-!- SUBUNIT: Isoform 1: Interacts with DLX1 (via homeobox DNA-binding
domain); this interaction suppresses DLX1-mediated transcriptional
activity in postnatal retina and enhances retinal ganglion cell
(RGC) differentiation (PubMed:21875655). Isoform 1: Interacts with
DLX2 (via homeobox DNA-binding domain); this interaction enhances
RGC differentiation (PubMed:21875655). Isoform 1: Interacts (via
C-terminus) with ISL1 (via C-terminus) (PubMed:24643061). Isoform
1 interacts with ISL2 (PubMed:24643061). Isoform 1: Interacts with
LHX2 (PubMed:24643061). Isoform 2: Interacts (via C-terminus) with
TP53 (via C-terminus) (PubMed:17145718). Isoform 2: Interacts with
POU4F1 isoform 1; this interaction inhibits both POU4F1 DNA-
binding and transcriptional activities (PubMed:8537352). Isoform 2
interacts (C-terminus) with ESR1 (via DNA-binding domain); this
interaction increases the estrogen receptor ESR1 transcriptional
activity in a DNA- and ligand 17-beta-estradiol-independent manner
(PubMed:9448000). {ECO:0000269|PubMed:17145718,
ECO:0000269|PubMed:21875655, ECO:0000269|PubMed:24643061,
ECO:0000269|PubMed:8537352, ECO:0000269|PubMed:9448000}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17668438,
ECO:0000269|PubMed:23805044}. Nucleus speckle
{ECO:0000250|UniProtKB:Q12837}. Cytoplasm
{ECO:0000269|PubMed:17668438}. Cell membrane
{ECO:0000269|PubMed:23805044}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Brn-3b-long {ECO:0000303|PubMed:8537352},
Brn-3b-l {ECO:0000303|PubMed:8537352};
IsoId=Q63934-1; Sequence=Displayed;
Name=2; Synonyms=Brn-3b {ECO:0000269|PubMed:8065921,
ECO:0000303|PubMed:7935408, ECO:0000303|PubMed:8162704,
ECO:0000303|PubMed:8290353}, Brn-3b-short
{ECO:0000303|PubMed:8537352}, Brn-3b-s
{ECO:0000303|PubMed:8537352};
IsoId=Q63934-2; Sequence=VSP_058838;
-!- TISSUE SPECIFICITY: Expressed in retinal ganglion cells (RGCs)
(PubMed:21875655, PubMed:23805044). Expressed in mature
osteoclasts (PubMed:17668438). Expressed in cardiomyocytes
(PubMed:18368538). Expressed in cells of layers of the superior
colliculus and the adjacent periaqueductal gray (PubMed:7691107).
Expressed in breast carcinoma (at protein level)
(PubMed:16152597). Expressed in the brain, peripheral sensory
nervous system and retina. Expressed in the optical, intermediate,
and deep gray areas of the superior colliculus, the dorsal column
of the mesencephalic and pontine central gray, and the lateral
interpeduncular nucleus of the brain. Expressed predominantly in
postmitotic, terminally differentiated neurons (PubMed:7904822).
Expressed in ganglion cell layer (GCL) of the retina
(PubMed:7691107, PubMed:23805044). {ECO:0000269|PubMed:16152597,
ECO:0000269|PubMed:17668438, ECO:0000269|PubMed:18368538,
ECO:0000269|PubMed:21875655, ECO:0000269|PubMed:23805044,
ECO:0000269|PubMed:7691107, ECO:0000269|PubMed:7904822}.
-!- DEVELOPMENTAL STAGE: Weakly expressed in the dorsal root ganglion
neurons at 10.5 dpc, the expression increases at least to 15.5 dpc
(PubMed:22326227). Expressed in the developing ganglion cell layer
of the retina at 12.5, 13.5 and 16.5 dpc (PubMed:8632990).
Expressed in the outer margin of the retina at 15.5 dpc
(PubMed:10414983). Isoform 1 and isoform 2 are expressed in
embryonic heart from 13.5 dpc until birth (at protein level)
(PubMed:18368538). Expressed in embryonic heart from 9.5 dpc until
birth (PubMed:18368538). Expressed in the developing spinal cord
from 13 dpc to postnatal day 1, not expressed in adults
(PubMed:8290353, PubMed:8537352). Expressed in retinal ganglion
cells at 13.5 dpc and peaks at 15.5 dpc to decline late in
development (PubMed:8637595). In the central nervous system,
selectively expressed in postmitotic, terminally differentiated
neurons (PubMed:7904822). {ECO:0000269|PubMed:10414983,
ECO:0000269|PubMed:18368538, ECO:0000269|PubMed:22326227,
ECO:0000269|PubMed:7904822, ECO:0000269|PubMed:8290353,
ECO:0000269|PubMed:8537352, ECO:0000269|PubMed:8632990,
ECO:0000269|PubMed:8637595}.
-!- INDUCTION: Up-regulated by the osteoclast differentiation factor
TNFSF11 (PubMed:17668438). Up-regulated by the steroid
dexamethasone (PubMed:8995448). Down-regulated upon neuronal
differentiation (PubMed:8995448). Down-regulated by serum
starvation (PubMed:8995448). Down-regulated in presence of
retinoic acid (PubMed:7904822). Down-regulated by dibutyryl cyclic
AMP (PubMed:8065921). {ECO:0000269|PubMed:17668438,
ECO:0000269|PubMed:7904822, ECO:0000269|PubMed:8065921,
ECO:0000269|PubMed:8995448}.
-!- DOMAIN: The transcriptional activation domain within the N-
terminal region is sufficient to induce transcriptional activity
(PubMed:8995448, PubMed:15733064). The transcriptional repression
domain containing the POU-specific domain and POU homeodomain is
necessary for DNA-binding activity and also sufficient to induce
transcriptional repression in a DNA-binding independent manner
(PubMed:8995448, PubMed:15733064). The polyhistidine repeat acts
as a targeting signal to nuclear speckles (By similarity).
{ECO:0000250|UniProtKB:Q12837, ECO:0000269|PubMed:15733064,
ECO:0000269|PubMed:8995448}.
-!- DISRUPTION PHENOTYPE: Mice develop to adulthood and are fertile
(PubMed:8637595). Display a thinner optic nerve (PubMed:8632990,
PubMed:10357904). Display a reduction in the number of retinal
ganglion cells (RGC) (PubMed:8637595, PubMed:8632990). Mice show
RGC axon guidance errors along the central visual pathways
(PubMed:10357904, PubMed:11163266). Dorsal root ganglion
projections in the spinal cord are normal (PubMed:22326227). Mice
show a decrease in expression levels for several genes involved in
the differentiation of RGCs (PubMed:24643061, PubMed:25775587).
Show an increase in DLX1 and DLX2 mRNA expression in the embryonic
retina, especially in the ganglion cell layer (PubMed:21875655).
{ECO:0000269|PubMed:10357904, ECO:0000269|PubMed:11163266,
ECO:0000269|PubMed:21875655, ECO:0000269|PubMed:22326227,
ECO:0000269|PubMed:24643061, ECO:0000269|PubMed:25775587,
ECO:0000269|PubMed:8632990, ECO:0000269|PubMed:8637595}.
-!- SIMILARITY: Belongs to the POU transcription factor family. Class-
4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S68377; AAC60672.1; -; mRNA.
EMBL; AK087546; BAC39921.1; -; mRNA.
EMBL; S69351; AAB30578.1; -; Genomic_DNA.
CCDS; CCDS22429.1; -. [Q63934-1]
RefSeq; NP_620394.2; NM_138944.2. [Q63934-1]
UniGene; Mm.234261; -.
ProteinModelPortal; Q63934; -.
SMR; Q63934; -.
BioGrid; 202311; 4.
STRING; 10090.ENSMUSP00000034115; -.
iPTMnet; Q63934; -.
PhosphoSitePlus; Q63934; -.
PaxDb; Q63934; -.
PRIDE; Q63934; -.
Ensembl; ENSMUST00000034115; ENSMUSP00000034115; ENSMUSG00000031688. [Q63934-1]
GeneID; 18997; -.
KEGG; mmu:18997; -.
UCSC; uc009mhy.1; mouse. [Q63934-1]
CTD; 5458; -.
MGI; MGI:102524; Pou4f2.
eggNOG; KOG1168; Eukaryota.
eggNOG; ENOG410XPNX; LUCA.
GeneTree; ENSGT00760000118935; -.
HOGENOM; HOG000116305; -.
HOVERGEN; HBG031829; -.
InParanoid; Q63934; -.
KO; K09366; -.
OMA; QYHAAMN; -.
OrthoDB; EOG091G0WBK; -.
PhylomeDB; Q63934; -.
TreeFam; TF316413; -.
Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
PRO; PR:Q63934; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031688; -.
CleanEx; MM_POU4F2; -.
Genevisible; Q63934; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0048675; P:axon extension; IGI:MGI.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
GO; GO:1990791; P:dorsal root ganglion development; IMP:UniProtKB.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:1902870; P:negative regulation of amacrine cell differentiation; IMP:UniProtKB.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:UniProtKB.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0045773; P:positive regulation of axon extension; IMP:UniProtKB.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:UniProtKB.
GO; GO:0043068; P:positive regulation of programmed cell death; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; IMP:UniProtKB.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:MGI.
GO; GO:0007605; P:sensory perception of sound; IGI:MGI.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
InterPro; IPR009057; Homeobox-like.
InterPro; IPR017970; Homeobox_CS.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR010982; Lambda_DNA-bd_dom.
InterPro; IPR013847; POU.
InterPro; IPR000327; POU_dom.
Pfam; PF00046; Homeobox; 1.
Pfam; PF00157; Pou; 1.
PRINTS; PR00028; POUDOMAIN.
SMART; SM00389; HOX; 1.
SMART; SM00352; POU; 1.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF47413; SSF47413; 1.
PROSITE; PS00027; HOMEOBOX_1; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
PROSITE; PS00035; POU_1; 1.
PROSITE; PS00465; POU_2; 1.
PROSITE; PS51179; POU_3; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Apoptosis; Cell membrane;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
DNA-binding; Homeobox; Membrane; Nucleus; Reference proteome;
Repressor; Transcription; Transcription regulation.
CHAIN 1 411 POU domain, class 4, transcription factor
2.
/FTId=PRO_0000100741.
DOMAIN 252 329 POU-specific. {ECO:0000255|PROSITE-
ProRule:PRU00530}.
DNA_BIND 347 406 Homeobox. {ECO:0000255|PROSITE-
ProRule:PRU00108}.
REGION 93 239 Transcriptional activation domain.
{ECO:0000269|PubMed:15733064}.
REGION 240 411 Transcriptional repression domain.
{ECO:0000269|PubMed:15733064}.
MOTIF 112 121 POU-IV box.
MOTIF 173 187 Nuclear speckle targeting signal.
{ECO:0000250|UniProtKB:Q12837}.
COMPBIAS 1 4 Poly-Met.
COMPBIAS 43 51 Poly-Ser.
COMPBIAS 54 67 Poly-Gly.
COMPBIAS 69 75 Poly-Ser.
COMPBIAS 76 85 Poly-Gly.
COMPBIAS 128 131 Poly-His.
COMPBIAS 157 160 Poly-Ser.
COMPBIAS 173 184 Poly-His.
VAR_SEQ 1 98 MMMMSLNSKQAFSMPHAGSLHVEPKYSALHSASPGSSAPAA
PSASSPSSSSNAGGGGGGGGGGGGGGRSSSSSSSGSGGSGG
GGGSEAMRRACLPTPP -> MCAFYLQLQ (in isoform
2).
/FTId=VSP_058838.
MUTAGEN 368 368 I->V: Stimulates induction of neurite
outgrowth and expression of synaptic
genes. Abolishes the inhibitory effect on
basal transcription and on gene
activation by POU4F1.
{ECO:0000269|PubMed:8662774,
ECO:0000269|PubMed:8972215,
ECO:0000269|PubMed:8995448,
ECO:0000269|PubMed:9261145,
ECO:0000269|PubMed:9694219}.
CONFLICT 404 405 RM -> KV (in Ref. 3; AAB30578).
{ECO:0000305}.
SEQUENCE 411 AA; 43173 MW; 97EA816F7DEC07C9 CRC64;
MMMMSLNSKQ AFSMPHAGSL HVEPKYSALH SASPGSSAPA APSASSPSSS SNAGGGGGGG
GGGGGGGRSS SSSSSGSGGS GGGGGSEAMR RACLPTPPSN IFGGLDESLL ARAEALAAVD
IVSQSKSHHH HPPHHSPFKP DATYHTMNTI PCTSAASSSS VPISHPSALA GTHHHHHHHH
HHHHQPHQAL EGELLEHLSP GLALGAMAGP DGTVVSTPAH APHMATMNPM HQAALSMAHA
HGLPSHMGCM SDVDADPRDL EAFAERFKQR RIKLGVTQAD VGSALANLKI PGVGSLSQST
ICRFESLTLS HNNMIALKPI LQAWLEEAEK SHREKLTKPE LFNGAEKKRK RTSIAAPEKR
SLEAYFAIQP RPSSEKIAAI AEKLDLKKNV VRVWFCNQRQ KQKRMKYSAG I


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